9ckx

Crystal structure of Dsk2 Sti1 domain bound to a transmembrane domain

Method: X-RAY DIFFRACTION Dmax: 77.2 Å Quality: EXCELLENT

1. Protein Identity and Related Structures Protein Identity & Related Structures

Ubiquitin-domain-containing protein,Response regulator FrzS,Vesicle-associated membrane protein 2

Homo sapiens

UniProt A0A1A0HF11

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 165–234 Chain B; UniProt 165–234 Mutation:I98A,I102A,I106A,I108A,I110A,I111A (Uniprot Vamp2 numbering) in the Vamp2 segment No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;2.5% MPD, 100 mM Tris pH 8.5 Resolution 1.98 Å R-free 0.232

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A1A0HF11_9ASCO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–74; UniProt 165–234 Author chain B; PDBConstruct 5–74; UniProt 165–234

Ubiquitin-domain-containing protein,Response regulator FrzS,Vesicle-associated membrane protein 2

Homo sapiens

UniProt A0AA46P9Z6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–124 Chain B; UniProt 2–124 Mutation:I98A,I102A,I106A,I108A,I110A,I111A (Uniprot Vamp2 numbering) in the Vamp2 segment No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;2.5% MPD, 100 mM Tris pH 8.5 Resolution 1.98 Å R-free 0.232

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0AA46P9Z6_MYXXA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 77–199; UniProt 2–124 Author chain B; PDBConstruct 77–199; UniProt 2–124

Ubiquitin-domain-containing protein,Response regulator FrzS,Vesicle-associated membrane protein 2

Homo sapiens

UniProt P63027

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 95–114 Chain B; UniProt 95–114 Mutation:I98A,I102A,I106A,I108A,I110A,I111A (Uniprot Vamp2 numbering) in the Vamp2 segment No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;2.5% MPD, 100 mM Tris pH 8.5 Resolution 1.98 Å R-free 0.232

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

6 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VAMP2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 203–222; UniProt 95–114 Author chain B; PDBConstruct 203–222; UniProt 95–114

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 9ckx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ckx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ckx
Deposition date deposition_date2024-07-10
Structure title titleCrystal structure of Dsk2 Sti1 domain bound to a transmembrane domain
Keywords keywordsMembrane protein Chaperone Sti1 Ubiquilin, CHAPERONE; CHAPERONE
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier25.77
Radius of gyration Rg (electron density) rg_electron25.05
Forward intensity I(0) i041862300.00
Molecular weight molecular_weight48741.0 kDa
Excluded volume excluded_volume60611 ų
Envelope volume envelope_volume73972 ų
Hydration-shell volume shell_volume25239 ų
Envelope diameter envelope_diameter81.4
Shell Rg shell_rg31.73
Envelope Rg envelope_rg25.14
Shape Rg shape_rg25.09
Total Rg total_rg25.66
Total atoms total_atoms6830
Residues n_residues444
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax77.2
Rg (real space) rg_real25.72
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real4.1860e+07
I(0) uncertainty (real space) i0_real_error5.4700e+05
Rg (reciprocal space) rg_reciprocal25.74
I(0) (reciprocal space) i0_reciprocal41860000.0000
Solution quality estimate total_estimate0.9109
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.9
Skewness Skewness skewness0.194
Kurtosis Kurtosis kurtosis-0.729
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14340000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.973; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)